The Chlamydia pneumoniae effector SemD exploits its host’s endocytic machinery by structural and functional mimicry

Kocher F, Applegate V, Reiners J, Port A, Spona D, Hänsch S, Mirzaiebadizi A, Ahmadian M, Smits S, Hegemann J, Mölleken K, Nature Communications 15(1) (2024) DOI

SASDTQ5 – SemDΔAPH (apo form)

Uncharacterized protein
MWexperimental 37 kDa
MWexpected 35 kDa
VPorod 67 nm3
log I(s) 3.22×103 3.22×102 3.22×101 3.22×100
Uncharacterized protein small angle scattering data  s, nm-1
ln I(s)
Uncharacterized protein Guinier plot ln 3.22×103 Rg: 2.8 nm 0 (2.8 nm)-2 s2
(sRg)2I(s)/I(0)
Uncharacterized protein Kratky plot 1.104 0 √3 sRg
p(r)
Uncharacterized protein pair distance distribution function Rg: 3.0 nm 0 Dmax: 10.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Uncharacterized protein CORAL model
Synchrotron SAXS data from solutions of SemDΔAPH in 137 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4, 3% glycerol, pH 8.5 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 100.00 μl sample at 8 mg/ml was injected at a 0.60 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 20°C. 2400 successive 0.995 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

AlphaFold Protein Structure Database, monomer: https://www.uniprot.org/uniprotkb/Q9Z7M7/entry

Uncharacterized protein (SemDΔAPH)
Mol. type   Protein
Organism   Chlamydia pneumoniae
Olig. state   Monomer
Mon. MW   35.1 kDa
 
UniProt   Q9Z7M7 (67-382)
Sequence   FASTA